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Conserved domains on  [gi|491167205|ref|WP_005025575|]
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methylated-DNA--[protein]-cysteine S-methyltransferase [Bilophila wadsworthia]

Protein Classification

methylated-DNA--[protein]-cysteine S-methyltransferase( domain architecture ID 1001076)

methylated-DNA--[protein]-cysteine S-methyltransferase repairs alkylated guanine in DNA by stoichiometrically transferring the alkyl group at the O-6 position to a cysteine residue in the enzyme, resulting in its irreversible inactivation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00901 super family cl35127
methylated-DNA--protein-cysteine methyltransferase; Provisional
4-153 4.24e-72

methylated-DNA--protein-cysteine methyltransferase; Provisional


The actual alignment was detected with superfamily member PRK00901:

Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 213.37  E-value: 4.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   4 FRETAFGRVGIEDKEGSITRLYLPGRSDAVS-EGPETALLGEAFAQLEAYFAGRRKTFDLPLRfDEGTPFMKQVWQALCT 82
Cdd:PRK00901   6 FYETPIGKIGIAENGTAITHLCFGEDKIPKDvTILETDLLKEANKQLEEYFEGKRKKFDLPLA-PQGTEFQKKVWKALQE 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491167205  83 VPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYG 153
Cdd:PRK00901  85 IPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEKENS 155
 
Name Accession Description Interval E-value
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
4-153 4.24e-72

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 213.37  E-value: 4.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   4 FRETAFGRVGIEDKEGSITRLYLPGRSDAVS-EGPETALLGEAFAQLEAYFAGRRKTFDLPLRfDEGTPFMKQVWQALCT 82
Cdd:PRK00901   6 FYETPIGKIGIAENGTAITHLCFGEDKIPKDvTILETDLLKEANKQLEEYFEGKRKKFDLPLA-PQGTEFQKKVWKALQE 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491167205  83 VPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYG 153
Cdd:PRK00901  85 IPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEKENS 155
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
6-155 1.40e-66

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 199.71  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   6 ETAFGRVGIEDKEGSITRLYLPGRSDAV-------SEGPETALLGEAFAQLEAYFAGRRKTFDLPLRFdEGTPFMKQVWQ 78
Cdd:COG0350    8 DTPLGPLLIAATDRGLCALSFGDDREEAllarfpaALREDPPLLAEAARQLDAYFAGERKDFDLPLDL-RGTPFQRRVWE 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491167205  79 ALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYGPA 155
Cdd:COG0350   87 ALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEGALAAA 163
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
71-150 3.27e-43

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 137.49  E-value: 3.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   71 PFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELER 150
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
70-149 8.65e-43

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 136.68  E-value: 8.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   70 TPFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELE 149
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
72-150 1.30e-37

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 123.36  E-value: 1.30e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491167205  72 FMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELER 150
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
 
Name Accession Description Interval E-value
PRK00901 PRK00901
methylated-DNA--protein-cysteine methyltransferase; Provisional
4-153 4.24e-72

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 234860 [Multi-domain]  Cd Length: 155  Bit Score: 213.37  E-value: 4.24e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   4 FRETAFGRVGIEDKEGSITRLYLPGRSDAVS-EGPETALLGEAFAQLEAYFAGRRKTFDLPLRfDEGTPFMKQVWQALCT 82
Cdd:PRK00901   6 FYETPIGKIGIAENGTAITHLCFGEDKIPKDvTILETDLLKEANKQLEEYFEGKRKKFDLPLA-PQGTEFQKKVWKALQE 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491167205  83 VPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYG 153
Cdd:PRK00901  85 IPYGETRSYKEIAVNIGNPKACRAVGLANNKNPIPIFIPCHRVIGANGKLVGYAGGLDIKEKLLKLEKENS 155
AdaB COG0350
DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, ...
6-155 1.40e-66

DNA repair enzyme Ada (O6-methylguanine-DNA--protein-cysteine methyltransferase) [Replication, recombination and repair];


Pssm-ID: 440119 [Multi-domain]  Cd Length: 163  Bit Score: 199.71  E-value: 1.40e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   6 ETAFGRVGIEDKEGSITRLYLPGRSDAV-------SEGPETALLGEAFAQLEAYFAGRRKTFDLPLRFdEGTPFMKQVWQ 78
Cdd:COG0350    8 DTPLGPLLIAATDRGLCALSFGDDREEAllarfpaALREDPPLLAEAARQLDAYFAGERKDFDLPLDL-RGTPFQRRVWE 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491167205  79 ALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYGPA 155
Cdd:COG0350   87 ALRKIPYGETVTYGELARAIGRPKAARAVGSACGANPIPIIIPCHRVIGADGSLGGYAGGLERKRALLELEGALAAA 163
DNA_binding_1 pfam01035
6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal ...
71-150 3.27e-43

6-O-methylguanine DNA methyltransferase, DNA binding domain; This is the C-terminal DNA-binding domain of 6-O-methylguanine-DNA methyltransferases.


Pssm-ID: 460036  Cd Length: 81  Bit Score: 137.49  E-value: 3.27e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   71 PFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELER 150
Cdd:pfam01035   1 PFQRRVWEALRQIPYGKTTTYGEIAKLLGRPKAARAVGNALGANPIPIIVPCHRVVGSDGSLGGYAGGLERKRALLELEG 80
ogt TIGR00589
O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are ...
70-149 8.65e-43

O-6-methylguanine DNA methyltransferase; All proteins in this family for which functions are known are involved alkyl-DNA transferases which remove alkyl groups from DNA as part of alkylation DNA repair. Some of the proteins in this family are also transcription regulators and have a distinct transcription regulatory domain. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273157  Cd Length: 80  Bit Score: 136.68  E-value: 8.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   70 TPFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELE 149
Cdd:TIGR00589   1 TPFQQKVWKALRTIPYGETKSYGQLAKAIGNPKAARAVGGANGRNPLAILVPCHRVVGKNGTLTGYGGGLERKEFLLEHE 80
ATase cd06445
The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT ...
72-150 1.30e-37

The DNA repair protein O6-alkylguanine-DNA alkyltransferase (ATase; also known as AGT, AGAT and MGMT) reverses O6-alkylation DNA damage by transferring O6-alkyl adducts to an active site cysteine irreversibly, without inducing DNA strand breaks. ATases are specific for repair of guanines with O6-alkyl adducts, however human ATase is not limited to O6-methylguanine, repairing many other adducts at the O6-position of guanine as well. ATase is widely distributed among species. Most ATases have N- and C-terminal domains. The C-terminal domain contains the conserved active-site cysteine motif (PCHR), the O6-alkylguanine binding channel, and the helix-turn-helix (HTH) DNA-binding motif. The active site is located near the recognition helix of the HTH motif. While the C-terminal domain of ATase contains residues that are necessary for DNA binding and alkyl transfer, the function of the N-terminal domain is still unknown. Removal of the N-terminal domain abolishes the activity of the C-terminal domain, suggesting an important structural role for the N-terminal domain in orienting the C-terminal domain for proper catalysis. Some ATase C-terminal domain homologs are either single-domain proteins that lack an N-terminal domain, or have a tryptophan substituted in place of the acceptor cysteine (i.e. the motif PCHR is replaced by PWHR). ATase null mutant mice are viable, fertile, and have a normal lifespan.


Pssm-ID: 119438 [Multi-domain]  Cd Length: 79  Bit Score: 123.36  E-value: 1.30e-37
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491167205  72 FMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELER 150
Cdd:cd06445    1 FQRRVWEALRQIPYGEVTTYGQIAKLAGTPKAARAVGSALARNPIPILIPCHRVVRSDGGLGGYRGGLERKRELLELEG 79
PRK10286 PRK10286
methylated-DNA--[protein]-cysteine S-methyltransferase;
48-149 1.72e-30

methylated-DNA--[protein]-cysteine S-methyltransferase;


Pssm-ID: 182355 [Multi-domain]  Cd Length: 171  Bit Score: 108.42  E-value: 1.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205  48 QLEAYFAGRRKTFDLPLRFDEGTPFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIG 127
Cdd:PRK10286  65 KLRDYFAGNLSIIDTLPTATGGTPFQREVWQTLRTIPCGQVMHYGQLAEQLGRPGAARAVGAANGSNPISIVVPCHRVIG 144
                         90       100
                 ....*....|....*....|..
gi 491167205 128 STGALVGYGGGLGMKERLLELE 149
Cdd:PRK10286 145 RNGTMTGYAGGVQRKEWLLRHE 166
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
47-152 9.84e-29

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 107.96  E-value: 9.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205  47 AQLEAYFAGRRKTFDLPLRFdEGTPFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRII 126
Cdd:PRK15435 247 REVIASLNQRDTPLTLPLDI-RGTAFQQQVWQALRTIPCGETVSYQQLANAIGKPKAVRAVASACAANKLAIVIPCHRVV 325
                         90       100
                 ....*....|....*....|....*.
gi 491167205 127 GSTGALVGYGGGLGMKERLLELERRY 152
Cdd:PRK15435 326 RGDGALSGYRWGVSRKAQLLRREAEN 351
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
1-155 1.04e-25

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 100.13  E-value: 1.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205   1 MLCFRETAFGRVGIE-DKEGSITRLYLPGRSDAVSEGPETALLGEAFAQLEAYFAGRRKTFDLPLRFDeGTPFMKQVWQA 79
Cdd:COG2169  201 LLLVAASARGVCAILlGDDPEALLRDLQDRFPAAELIGGDAAFEQLVAEVVGFVEGPLLGLDLPLDLR-GTAFQQRVWQA 279
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491167205  80 LCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGALVGYGGGLGMKERLLELERRYGPA 155
Cdd:COG2169  280 LRAIPAGETASYAEIAARIGAPKAVRAVAAACAANQLAVAIPCHRVVRADGALSGYRWGVERKRALLEREAAAAAA 355
Atl1 COG3695
Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like ...
70-149 2.14e-15

Alkylated DNA nucleotide flippase Atl1, participates in nucleotide excision repair, Ada-like DNA-binding domain [Transcription];


Pssm-ID: 442910  Cd Length: 104  Bit Score: 67.52  E-value: 2.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205  70 TPFMKQVWQALCTVPYAHTASYKDIAEAVGNPKACRAVGMANNRNPIAIIVPCHRIIGSTGAL-VGYGGGLGMKERLLEL 148
Cdd:COG3695    4 EEFYERVYEVVAQIPPGRVATYGDIAALAGLPRGARQVGRALRALPEGSDLPWHRVVNADGRLsPGHAGGAEEQRELLEA 83

                 .
gi 491167205 149 E 149
Cdd:COG3695   84 E 84
PRK03887 PRK03887
methylated-DNA--protein-cysteine methyltransferase; Provisional
64-149 6.75e-10

methylated-DNA--protein-cysteine methyltransferase; Provisional


Pssm-ID: 167628 [Multi-domain]  Cd Length: 175  Bit Score: 54.74  E-value: 6.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491167205  64 LRFDEGTPFMKQVWQALC-TVPYAHTASYKDIAEAVGNpkACRAVGMANNRNPIAIIVPCHRIIGSTGALVgYGGGLGMK 142
Cdd:PRK03887  85 LSFEGLTPFERKVYEWLTkNVKRGEVITYGELAKALNT--SPRAVGGAMKRNPYPIIVPCHRVVGRKNPGL-YTPKPEYK 161

                 ....*..
gi 491167205 143 ERLLELE 149
Cdd:PRK03887 162 KFLLEVE 168
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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